FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2009593046> ?p ?o ?g. }

• W2009593046 endingPage "2482" @default.
• W2009593046 startingPage "2470" @default.
• W2009593046 abstract "High-sensitivity differential scanning calorimetry and Fourier transform infrared spectroscopy were used to study the interaction of a cationic α-helical transmembrane peptide, acetyl-Lys2-Leu24-Lys2-amide (L24), and members of the homologous series of zwitterionic n-saturated diacyl phosphatidylethanolamines (PEs). Analogs of L24, in which the lysine residues were replaced by 2,3-diaminopropionic acid (acetyl-DAP2-Leu24-DAP2-amide (L24DAP)) or in which a leucine residue at each end of the polyleucine sequence was replaced by a tryptophan (Ac-K2-W-L22-W-K2-amide (WL22W)), were also studied to investigate the roles of lysine side-chain snorkeling and aromatic side-chain interactions with the interfacial region of phospholipid bilayers. The gel/liquid-crystalline phase transition temperature of the PE bilayers is altered by these peptides in a hydrophobic mismatch-independent manner, in contrast to the hydrophobic mismatch-dependent manner observed previously with zwitterionic phosphatidylcholine (PC) and anionic phosphatidylglycerol (PG) bilayers. Moreover, all three peptides reduce the phase transition temperature to a greater extent in PE bilayers than in PC and PG bilayers, indicating a greater disruption of PE gel-phase bilayer organization. Moreover, the lysine-anchored L24 reduces the phase transition temperature, enthalpy, and the cooperativity of PE bilayers to a much greater extent than DAP-anchored L24DAP, whereas replacement of the terminal leucines by tryptophan residues (Ac-K2-W-L22-W-K2-amide) only slightly attenuates the effects of this peptide on the chain-melting phase transition of the host PE bilayers. All three peptides form very stable α-helices in PE bilayers, but small conformational changes occur in response to mismatch between peptide hydrophobic length and gel-state lipid bilayer hydrophobic thickness. These results suggest that the lysine snorkeling plays a significant role in the peptide-PE interactions and that cation-π-interactions between lysine and tryptophan residues may modulate these interactions. Altogether, these results suggest that the lipid-peptide interactions are affected not only by the hydrophobic mismatch between these peptides and the host lipid bilayer but also by the electrostatic and hydrogen-bonding interactions between the positively charged lysine residues at the termini of these peptides and the polar headgroups of PE bilayers." @default.
• W2009593046 created "2016-06-24" @default.
• W2009593046 creator A5004374190 @default.
• W2009593046 creator A5052295449 @default.
• W2009593046 creator A5060470951 @default.
• W2009593046 creator A5077109450 @default.
• W2009593046 date "2004-10-01" @default.
• W2009593046 modified "2023-10-12" @default.
• W2009593046 title "Effect of Variations in the Structure of a Polyleucine-Based α-Helical Transmembrane Peptide on Its Interaction with Phosphatidylethanolamine Bilayers" @default.
• W2009593046 cites W1967125556 @default.
• W2009593046 cites W1968028474 @default.
• W2009593046 cites W1969025574 @default.
• W2009593046 cites W1976086178 @default.
• W2009593046 cites W1977986845 @default.
• W2009593046 cites W1979761938 @default.
• W2009593046 cites W1981261838 @default.
• W2009593046 cites W1984292994 @default.
• W2009593046 cites W2001806196 @default.
• W2009593046 cites W2015060049 @default.
• W2009593046 cites W2015258557 @default.
• W2009593046 cites W2016229337 @default.
• W2009593046 cites W2022952909 @default.
• W2009593046 cites W2024156929 @default.
• W2009593046 cites W2026935659 @default.
• W2009593046 cites W2027305112 @default.
• W2009593046 cites W2030210434 @default.
• W2009593046 cites W2032786770 @default.
• W2009593046 cites W2040211368 @default.
• W2009593046 cites W2040585305 @default.
• W2009593046 cites W2045566035 @default.
• W2009593046 cites W2048767858 @default.
• W2009593046 cites W2056288818 @default.
• W2009593046 cites W2057233697 @default.
• W2009593046 cites W2057499497 @default.
• W2009593046 cites W2061124406 @default.
• W2009593046 cites W2063036753 @default.
• W2009593046 cites W2077471821 @default.
• W2009593046 cites W2083767996 @default.
• W2009593046 cites W2084543459 @default.
• W2009593046 cites W2087030908 @default.
• W2009593046 cites W2088694643 @default.
• W2009593046 cites W2092393875 @default.
• W2009593046 cites W2104534420 @default.
• W2009593046 cites W2113301046 @default.
• W2009593046 cites W2114471659 @default.
• W2009593046 cites W2133610281 @default.
• W2009593046 cites W2135585405 @default.
• W2009593046 cites W2139875556 @default.
• W2009593046 cites W2143815964 @default.
• W2009593046 cites W2150384032 @default.
• W2009593046 cites W3010233924 @default.
• W2009593046 cites W3025109026 @default.
• W2009593046 cites W4248208651 @default.
• W2009593046 doi "https://doi.org/10.1529/biophysj.104.046342" @default.
• W2009593046 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1304667" @default.
• W2009593046 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15454444" @default.
• W2009593046 hasPublicationYear "2004" @default.
• W2009593046 type Work @default.
• W2009593046 sameAs 2009593046 @default.
• W2009593046 citedByCount "38" @default.
• W2009593046 countsByYear W20095930462012 @default.
• W2009593046 countsByYear W20095930462013 @default.
• W2009593046 countsByYear W20095930462014 @default.
• W2009593046 countsByYear W20095930462016 @default.
• W2009593046 countsByYear W20095930462017 @default.
• W2009593046 countsByYear W20095930462018 @default.
• W2009593046 countsByYear W20095930462019 @default.
• W2009593046 countsByYear W20095930462021 @default.
• W2009593046 countsByYear W20095930462022 @default.
• W2009593046 crossrefType "journal-article" @default.
• W2009593046 hasAuthorship W2009593046A5004374190 @default.
• W2009593046 hasAuthorship W2009593046A5052295449 @default.
• W2009593046 hasAuthorship W2009593046A5060470951 @default.
• W2009593046 hasAuthorship W2009593046A5077109450 @default.
• W2009593046 hasBestOaLocation W20095930461 @default.
• W2009593046 hasConcept C12554922 @default.
• W2009593046 hasConcept C178790620 @default.
• W2009593046 hasConcept C185592680 @default.
• W2009593046 hasConcept C192157962 @default.
• W2009593046 hasConcept C2776330855 @default.
• W2009593046 hasConcept C2776706248 @default.
• W2009593046 hasConcept C2778439535 @default.
• W2009593046 hasConcept C2778918659 @default.
• W2009593046 hasConcept C2779281246 @default.
• W2009593046 hasConcept C2781170229 @default.
• W2009593046 hasConcept C39944091 @default.
• W2009593046 hasConcept C41625074 @default.
• W2009593046 hasConcept C515207424 @default.
• W2009593046 hasConcept C55493867 @default.
• W2009593046 hasConcept C71240020 @default.
• W2009593046 hasConcept C8010536 @default.
• W2009593046 hasConcept C86803240 @default.
• W2009593046 hasConceptScore W2009593046C12554922 @default.
• W2009593046 hasConceptScore W2009593046C178790620 @default.
• W2009593046 hasConceptScore W2009593046C185592680 @default.
• W2009593046 hasConceptScore W2009593046C192157962 @default.
• W2009593046 hasConceptScore W2009593046C2776330855 @default.
• W2009593046 hasConceptScore W2009593046C2776706248 @default.

• next